Structural principles controlling HIV envelope glycosylation.

TitleStructural principles controlling HIV envelope glycosylation.
Publication TypeJournal Article
Year of Publication2017
AuthorsBehrens A-J, Crispin M
JournalCurr Opin Struct Biol
Volume44
Pagination125-133
Date Published06/01/2017
ISSN1879-033X
Abstract

The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive 'trimer-induced mannose patch'. Importantly, the immature glycans present a highly conserved feature of the virus that is targeted by broadly neutralizing antibodies. Quantitative mass spectrometry of glycopeptides together with structures of the trimeric viral-spike define the steric principles controlling processing and provide a detailed map of the glycan shield.

DOI10.1016/j.sbi.2017.03.008
Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID28363124
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